MolNFT v1 · #182522 · protein
Crystal structure of the catalytic domain of the inosine monophosphate dehydrogenase from bacillus anthracis in the complex with imp and the inhibitor P221
7MTU · Inosine-5'-monophosphate dehydrogenase: “Crystal structure of the catalytic domain of the inosine monophosphate dehydrogenase from bacillus anthracis…”. X-ray diffraction, 3 ligands (IMP, ZO7, K), 20 pockets (best druggability…
- PDB
- 7MTU
- Type
- protein
- Length
- 2,794 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Inosine-5'-monophosphate dehydrogenase
- EC
- 1.1.1.205
- UniProt
- A0A6H3A7R4
- Ligands
- IMP, ZO7, K
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 7 distinct chains · 37% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, H | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 349 | 37% helix, 21% strand | A0A6H3A7R4 |
| B | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 350 | 37% helix, 22% strand | A0A6H3A7R4 |
| C | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 351 | 37% helix, 21% strand | A0A6H3A7R4 |
| D | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 349 | 38% helix, 21% strand | A0A6H3A7R4 |
| E | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 347 | 36% helix, 20% strand | A0A6H3A7R4 |
| F | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 348 | 35% helix, 22% strand | A0A6H3A7R4 |
| G | Inosine-5'-monophosphate dehydrogenase (EC 1.1.1.205) | protein | 351 | 37% helix, 21% strand | A0A6H3A7R4 |
Ligands and binding sites
- IMP · Inosinic acid · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- ZO7 · N-{2-chloro-5-[({2-[3-(prop-1-en-2-yl)phenyl]propan-2-yl}carbamoyl)amino]phenyl}-beta-D-arabinopyranosylamine · ligand · 8 copies · chains A, C, B, D, E, G, F, H
- K · Potassium ion · metal · 9 copies · chains A, B, D, C, E, F, H, G
- GOL · Glycerol · additive · 6 copies · chains A, C, H
- EDO · 1,2-ethanediol · additive · chains F, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1012 | 0.81 | 0.82 | 103 | IMP, ZO7 |
| 2 | 1020 | 0.80 | 0.81 | 104 | IMP, ZO7 |
| 3 | 923 | 0.80 | 0.82 | 87 | IMP, ZO7 |
| 4 | 887 | 0.79 | 0.82 | 87 | IMP, ZO7 |
| 5 | 598 | 0.78 | 0.84 | 55 | IMP, ZO7 |
Interfaces
14 interfaces between chains.
- G–H · 2647 Ų buried · 46 hydrogen bonds · protein-protein
- B–D · 2640 Ų buried · 47 hydrogen bonds · protein-protein
- A–B · 2632 Ų buried · 45 hydrogen bonds · protein-protein
- E–G · 2605 Ų buried · 46 hydrogen bonds · protein-protein
- A–C · 2604 Ų buried · 41 hydrogen bonds · protein-protein
Compared structures
- 7MTU · Crystal Structure of the Catalytic Domain of the Inosine Monophosphate Dehydrogenase from… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt A0A6H3A7R4
- Elsewhere: RCSB PDB 7MTU · PDBe 7MTU · UniProt A0A6H3A7R4
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